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A novel super‐secondary structure of proteins and the relation between the structure and the amino acid sequence
Author(s) -
Efimov A.V.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80039-3
Subject(s) - protein secondary structure , sequence (biology) , amino acid , peptide sequence , chemistry , protein primary structure , folding (dsp implementation) , amino acid residue , peptide , protein folding , protein structure , glycine , crystallography , stereochemistry , biochemistry , gene , electrical engineering , engineering
A novel protein super‐secondary structure which is referred to as an αα‐corner is considered. The αα‐corner is formed by two consecutive α‐helices packed approximately crosswise and connected by two or more peptide units. It is shown that the amino acid sequences coding for the αα‐corners have a strictly definite order of hydrophobic, hydrophilic and glycine residues. A hypothesis is suggested that the αα‐corner can be an embryo of protein folding.